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Entry: A0A1A7QJI1_9SPHN
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ID   A0A1A7QJI1_9SPHN        Unreviewed;       516 AA.
AC   A0A1A7QJI1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132};
GN   ORFNames=A9995_09450 {ECO:0000313|EMBL:OBX18787.1};
OS   Erythrobacter sp. QSSC1-22B.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1860125 {ECO:0000313|EMBL:OBX18787.1, ECO:0000313|Proteomes:UP000092728};
RN   [1] {ECO:0000313|EMBL:OBX18787.1, ECO:0000313|Proteomes:UP000092728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSSC1-22B {ECO:0000313|EMBL:OBX18787.1,
RC   ECO:0000313|Proteomes:UP000092728};
RA   Bowman J.P.;
RT   "Draft genome of Erythrobacter sp. QSSC1-22B.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBX18787.1}.
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DR   EMBL; LZRP01000005; OBX18787.1; -; Genomic_DNA.
DR   RefSeq; WP_067612062.1; NZ_LZRP01000005.1.
DR   AlphaFoldDB; A0A1A7QJI1; -.
DR   STRING; 1860125.A9995_09450; -.
DR   OrthoDB; 9761719at2; -.
DR   Proteomes; UP000092728; Unassembled WGS sequence.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF9; CATALASE; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038928-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092728}.
FT   DOMAIN          10..396
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         343
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-2"
SQ   SEQUENCE   516 AA;  58274 MW;  E9E60E9B84FAF8A0 CRC64;
     MADKSIPPTT TDAGIRVQSD EHSLTLGPDG PIVLNDHYLI EQMANFNRER IPERQPHAKG
     SGAFGHFEAT ADITKYTKAR FFQPGTKTDV AMRFSTVAGE RGSPDTWRDP RGFSVKFYTE
     DGNFDMVGNN TPIFFVRDPM KFQHFIRSQK RRADNGLRDH DMMWDFWTLS PESAHQVTYL
     MGDRGVPKNW REMNGYGSHT YMLINEDGEK FWVKWHFHTD VGGMSGNAHL TQDEAVKTAG
     EDSDYHRRDL FDAISDGDFP SWTLKFQIMP YDDAKTYRIN PFDLTKTWPH EDYPLIEVGR
     LTLNENPVDW DTQIEQLAFE PNNMVPGLGL SPDKMLLARG FAYADAHRHR LGVNYKQIPV
     NAARNAQVNS YSRAGAMRTV NAVDPVYAPN SYGGPAAQPE VGGEATWYAD GDMVRQAYTL
     REDDDDWSQP RALINEVMDG AQRDRFVSNV AGHLADGVSE SVLIRAFKYW RNVDDAIGER
     IEKTVRDKIG GRSKAPGMAS AKSISDEGQA KRPNKS
//
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